Inspecting fluctuation and coordination around chromophore inside green fluorescent protein from water to nonpolar solvent
نویسندگان
چکیده
منابع مشابه
Chromophore formation in green fluorescent protein.
The green fluorescent protein (GFP) from the jellyfish Aequorea Victoria forms an intrinsic chromophore through cyclization and oxidation of an internal tripeptide motif [Prasher, D. C., et al. (1992) Gene 111, 229-233; Cody, C. E., et al. (1993) Biochemistry 32, 1212-1218]. We monitored the formation of the chromophore in vitro using the S65T-GFP chromophore mutant. S65T-GFP recovered from inc...
متن کاملOn the photodetachment from the green fluorescent protein chromophore.
Motivated by the discrepancies in recent experimental and theoretical studies of photodetachment from isolated model chromophores of the green fluorescent protein (GFP), this study reports calculations of the electron detachment energies and photoelectron spectra of the phenolate and deprotonated p-hydroxybenzylidene-2,3-dimethylimidazolinone (HBDI) anions. The spectra were computed using doubl...
متن کاملDeactivation mechanism of the green fluorescent chromophore.
We report time-resolved fluorescence data for the anion of p-hydroxybenzylidene dimethylimidazolinone (p-HBDI), a model chromophore of the green fluorescence protein, in viscous glycerol-water mixtures over a range of temperatures, T. The markedly nonexponential decay of the excited electronic state is interpreted with the aid of an inhomogeneous model possessing a Gaussian coordinate-dependent...
متن کاملEffect of protein environment on electronically excited and ionized states of the green fluorescent protein chromophore.
The effect of the protein environment on the electronic structure of the green fluorescent protein (GFP) chromophore is investigated by QM/MM (quantum mechanics/molecular mechanics) calculations. The protein has very small effect on the excitation energy of the bright absorbing and the lowest triplet states of the anionic GFP chromophore, deprotonated 4-hydroxybenzylidene-2,3-dimethylimidazolin...
متن کاملPhotophysics and Dihedral Freedom of the Chromophore in Yellow, Blue, and Green Fluorescent Protein
Green fluorescent protein (GFP) and GFP-like fluorescent proteins owe their photophysical properties to an autocatalytically formed intrinsic chromophore. According to quantum mechanical calculations, the excited state of chromophore model systems has significant dihedral freedom, which may lead to fluorescence quenching intersystem crossing. Molecular dynamics simulations with freely rotating ...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Proteins: Structure, Function, and Bioinformatics
سال: 2019
ISSN: 0887-3585,1097-0134
DOI: 10.1002/prot.25676